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Conserved domains on  [gi|26986617|ref|NP_758498|]
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extracellular sulfatase Sulf-1 precursor [Mus musculus]

Protein Classification

G6S and DUF3740 domain-containing protein( domain architecture ID 10888354)

G6S and DUF3740 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


:

Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 544.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147   1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147  81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                       330       340       350
                ....*....|....*....|....*....|
gi 26986617 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 3.82e-69

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


:

Pssm-ID: 463628  Cd Length: 142  Bit Score: 225.30  E-value: 3.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617   612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548  76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
767-816 9.85e-19

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


The actual alignment was detected with superfamily member cd16147:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 396  Bit Score: 89.53  E-value: 9.85e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 26986617 767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 816
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 544.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147   1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147  81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                       330       340       350
                ....*....|....*....|....*....|
gi 26986617 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 2.52e-75

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 251.34  E-value: 2.52e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVelGSLQVMNKTR-------KIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsS 114
Cdd:COG3119  23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--Y 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 115 PSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDL 194
Cdd:COG3119  98 NGGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 195 ITNESINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmef 274
Cdd:COG3119 133 LTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 275 tnvLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGS 353
Cdd:COG3119 198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGS 274
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26986617 354 IVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119 275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 3.82e-69

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 225.30  E-value: 3.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617   612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548  76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
Sulfatase pfam00884
Sulfatase;
43-374 8.13e-49

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 174.92  E-value: 8.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617    43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884   1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   197 NESINYfkmskRMYPHRPIMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   277 vlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGP-SIEPG 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPgGKAKG 276
                         330       340
                  ....*....|....*....|..
gi 26986617   353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 1.16e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 120.93  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759   6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759  83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEftnVLQRKRLQTLMS---VDDSVERLYNMLVESGELDNTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDL 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                 ....*.
gi 26986617  392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
767-816 9.85e-19

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 89.53  E-value: 9.85e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 26986617 767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 816
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 544.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147   1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147  81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147 160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                       330       340       350
                ....*....|....*....|....*....|
gi 26986617 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
42-414 1.36e-87

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 285.19  E-value: 1.36e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQ--DVeLGSLQ-VMNKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSP 115
Cdd:cd16031   2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLI 195
Cdd:cd16031  79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDII 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 196 TNESINYFKmsKRMyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQ 262
Cdd:cd16031 149 TDKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLD 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 263 YtgpmlPIHMEFTnvLQR--KR-LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16031 224 G-----RFDTPEK--YQRymKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIR 295
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26986617 340 VPFFIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDlekpgnrfrtNKKAKIWRDTFLVE 414
Cdd:cd16031 296 VPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 2.52e-75

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 251.34  E-value: 2.52e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVelGSLQVMNKTR-------KIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsS 114
Cdd:COG3119  23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--Y 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 115 PSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDL 194
Cdd:COG3119  98 NGGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 195 ITNESINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmef 274
Cdd:COG3119 133 LTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 275 tnvLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGS 353
Cdd:COG3119 198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGS 274
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26986617 354 IVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119 275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 3.82e-69

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 225.30  E-value: 3.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617   612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548  76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
43-384 1.43e-53

sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 186.10  E-value: 1.43e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQ---DVE-LGSLQVmnKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcssp 115
Cdd:cd16022   1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHgfdyakdyftdli 195
Cdd:cd16022  74 GGGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 196 tNESINYFKmskRMYPHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeft 275
Cdd:cd16022 103 -DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------FAYYAMVS------------------- 138
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 276 nvlqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGSI 354
Cdd:cd16022 139 ------------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQV 206
                       330       340       350
                ....*....|....*....|....*....|
gi 26986617 355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-389 1.34e-52

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 188.93  E-value: 1.34e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDD---QDveLGSLQVMN-KTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSP 115
Cdd:cd16034   1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SwqamHEPRTFAVYLNNTGYRTAFFGKY-LNE-------YNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16034  76 P----PDAPTIADVLKDAGYRTGYIGKWhLDGperndgrADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 184 FDYAKDYFTDLItnesINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----K 257
Cdd:cd16034 152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 258 HWIMQYtgpmlpihmeFTNVLqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFD 337
Cdd:cd16034 224 EDLRGY----------YAMIT---------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEES 283
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 26986617 338 IRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16034 284 IRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLL 336
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
43-397 1.31e-49

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 179.63  E-value: 1.31e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVELGSlqVMN---KTRKIME--QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPS 116
Cdd:cd16027   1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLIT 196
Cdd:cd16027  79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 197 NE----SINYFkmskrmYPHRPIMMVISHAAPHGPEDsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpi 270
Cdd:cd16027 141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPdtPEVREDLADYYD------ 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 271 hmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-I 349
Cdd:cd16027 194 --------------EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 26986617 350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
Sulfatase pfam00884
Sulfatase;
43-374 8.13e-49

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 174.92  E-value: 8.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617    43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884   1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   197 NESINYfkmskRMYPHRPIMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   277 vlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGP-SIEPG 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPgGKAKG 276
                         330       340
                  ....*....|....*....|..
gi 26986617   353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-389 4.24e-47

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 173.88  E-value: 4.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDD---QDVelgSLQvMNKtrkIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYT---- 107
Cdd:cd16144   1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipg 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 108 ------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRN 176
Cdd:cd16144  74 rrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 177 GIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMD 256
Cdd:cd16144 152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 257 KHWIMQYTGPMLpihmeftnvlqrkrlqtlMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-------KG 329
Cdd:cd16144 218 KGQKNPVYAAMI------------------ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26986617 330 KSMPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLKLL 389
Cdd:cd16144 280 KGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPlpPPQHLDGVSLVPLL 342
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-414 1.45e-46

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 172.02  E-value: 1.45e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDV----ELGSLQVmnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16033   1 PNILFIMTDQQRYdtlgCYGNPIV--KTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKDY 190
Cdd:cd16033  79 RGLPPGVETFSEDLREAGYRNGYVGK-------------WH---------------VGPEETPLDYGFDEylpvetTIEY 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 191 FTDLITNESINYFKMSKRmyphrPIMMVISHAAPHGPEDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPMLP 269
Cdd:cd16033 131 FLADRAIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKRW 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 270 IHMEFTNVLQRKRLQ------TLMsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPF 342
Cdd:cd16033 203 GVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPL 279
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26986617 343 FIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtnkkakiWRDTFLVE 414
Cdd:cd16033 280 IIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
43-400 1.83e-40

uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293765 [Multi-domain]  Cd Length: 409  Bit Score: 154.24  E-value: 1.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVelGSLQVMN----KT---RKIMEQGgATFTNaFVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSP 115
Cdd:cd16146   1 PNVILILTDDQGY--GDLGFHGnpilKTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWH-----TIL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL-----------IKNSRFYNyTVCRNGIKEK 181
Cdd:cd16146  72 GRERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKFVK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 182 HgfdyaKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYApnmdkhwim 261
Cdd:cd16146 151 T-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 262 qytgpMLpihmefTNvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKGKSMPYDF 336
Cdd:cd16146 213 -----MI------EN------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617 337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLLDLEKPGNRFRT 400
Cdd:cd16146 270 GHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLLKGESDPWPERT 336
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-398 2.79e-40

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 151.16  E-value: 2.79e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 151
Cdd:cd16037  36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 152 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSA 231
Cdd:cd16037 104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 232 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnvlqRKRLQT----LMS-VDDSVERLYNMLVESGEL 306
Cdd:cd16037 150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 307 DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVL 386
Cdd:cd16037 189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
                       330
                ....*....|..
gi 26986617 387 KLLDLEKPGNRF 398
Cdd:cd16037 268 PLAEGPDDPDRV 279
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-389 5.47e-39

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 150.05  E-value: 5.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDV-ELGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQ 118
Cdd:cd16145   1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 119 AmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWLG--------------LIKNSR--FYNYTVCRNGIK 179
Cdd:cd16145  81 P--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 180 EKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhw 259
Cdd:cd16145 159 GNNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ-- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 260 imqytgpmlpihmeftnvlQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHI-------GQF-----GL 326
Cdd:cd16145 229 -------------------PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPL 289
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26986617 327 VKGK-SMpYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16145 290 RGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 5.48e-39

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 148.87  E-value: 5.48e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVE----LGSLQVmnKTRKI--MEQGGATFTNAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNEN 111
Cdd:cd16155   2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 112 CSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdyf 191
Cdd:cd16155  77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 192 tdliTNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIH 271
Cdd:cd16155 108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 272 MEFT--------NVlqRKRLQ----TLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16155 174 DEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMR 250
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26986617 340 VPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16155 251 VPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 5.95e-38

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 146.22  E-value: 5.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQ--DVeLGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPS 116
Cdd:cd16152   1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 wqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLit 196
Cdd:cd16152  78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 197 neSINYfkMSKRMyPHRPIMMVISHAAPH---------GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkh 258
Cdd:cd16152 113 --AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL-PDY--------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 259 wimqytgpmlpihmeftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHigqFGLVKG--KSMPYDF 336
Cdd:cd16152 178 ------------------------LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26986617 337 DIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16152 231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
42-390 4.36e-35

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 139.24  E-value: 4.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVELGSLQvmnktRKIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNencs 113
Cdd:cd16030   2 KPNVLFIAVDDLRPWLGCYG-----GHPAKtpnidrlaARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 114 SPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG-------- 183
Cdd:cd16030  73 SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawea 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 184 FDYAKDYFTD-LITNESINYFKMSKRMypHRPIMMVISHAAPHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPNm 255
Cdd:cd16030 153 ADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 256 DKHWIMQYTGPMLPIHMEFTNVL----QRKRLQT-LMSV---DDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV 327
Cdd:cd16030 229 DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHW 308
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26986617 328 kGKSMPYDFDIRVPFFIRGPSI-EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:cd16030 309 -GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
74-411 1.80e-34

Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.


Pssm-ID: 293752 [Multi-domain]  Cd Length: 449  Bit Score: 137.78  E-value: 1.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 142
Cdd:cd16028  36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 143 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPIMMVI 219
Cdd:cd16028 109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 220 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNV-----LQRKRLQ 284
Cdd:cd16028 164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 285 T----LMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIE----PGSIV 355
Cdd:cd16028 238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26986617 356 PQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtNKKAKIWRDTF 411
Cdd:cd16028 317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-387 2.41e-34

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 132.67  E-value: 2.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTD----DQdvelgsLQVMNKTRKIM------EQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVytnnenc 112
Cdd:cd16148   1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 113 sspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSYIPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDY 190
Cdd:cd16148  68 ----WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPHLFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDE 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 191 FTDLITNESINYFKmskRMYPHRPIMMVISHAAPHGPEdsapqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpI 270
Cdd:cd16148 129 RAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--------LYDAE----------------------------V 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 271 HMeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSI 349
Cdd:cd16148 170 RY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGK 233
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 26986617 350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLK 387
Cdd:cd16148 234 EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-389 4.34e-34

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293750 [Multi-domain]  Cd Length: 399  Bit Score: 135.38  E-value: 4.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQ---DVE-LGSlqVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNE 110
Cdd:cd16026   1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 111 NCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGI 178
Cdd:cd16026  79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMEN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 179 KEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsynyapnmdkh 258
Cdd:cd16026 153 EEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFASEKFK----GRSGA-------------- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 259 wimqytGPmlpihmeFTNVLQrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHG--YHIGQFG-----LVKGKS 331
Cdd:cd16026 211 ------GL-------YGDVVE--------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKG 269
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26986617 332 MPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLL 389
Cdd:cd16026 270 TTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRviDGKDISPLL 330
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
72-390 5.61e-34

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 133.09  E-value: 5.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  72 QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 151
Cdd:cd16032  34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 152 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPIMMVISHAAP 224
Cdd:cd16032  99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 225 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESG 304
Cdd:cd16032 145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 305 ELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV---D 381
Cdd:cd16032 189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267

                ....*....
gi 26986617 382 GKSVLKLLD 390
Cdd:cd16032 268 GRSLLPLLE 276
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-423 9.16e-34

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 134.25  E-value: 9.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDqdVELGSLQVMNKTRKI-------MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16143   1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWqaMHEPR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDY 186
Cdd:cd16143  79 PL--IEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 187 akdYFT-------DLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDK 257
Cdd:cd16143 145 ---YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGP 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 258 H--WIMQytgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSM 332
Cdd:cd16143 203 YgdFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDP 256
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 333 PYDF-----DI-----RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLLdlekpgnrfr 399
Cdd:cd16143 257 SGPLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL---------- 326
                       410       420
                ....*....|....*....|....*..
gi 26986617 400 TNKKAKIWRDTFLVE--RGKF-LRKKE 423
Cdd:cd16143 327 LGPKKQEVRESLVHHsgNGSFaIRKGD 353
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-386 4.40e-31

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 122.73  E-value: 4.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDV----ELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV-----YTNNENCS 113
Cdd:cd16149   1 PNILFILTDDQGPwalgCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 114 SP-SWQAMHEprTFAVYLNNTGYRTAFFGKylneyngsyippgwreW-LGliknsrfynytvcrngikekhgfDYAKDYF 191
Cdd:cd16149  81 KPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WhLG-----------------------DDAADFL 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 192 TDLITNEsinyfkmskrmyphRPIMMVISHAAPHGPedsapqfsklypnasqhitpsynyapnmdkhWimQYtgpmlpih 271
Cdd:cd16149 120 RRRAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY-------- 144
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 272 meftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFI 344
Cdd:cd16149 145 -----------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFII 211
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 26986617 345 RGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD--GKSVL 386
Cdd:cd16149 212 RWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-378 4.47e-31

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 124.24  E-value: 4.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQ----DVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-W 117
Cdd:cd16035   1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 118 QAMHEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLIT 196
Cdd:cd16035  78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 197 NESINY-FKMSKRMYPHRPIMMVISHAAPHgpeDsapqfsklypnasqhItpsyNYAPNMDKHWImqytgpmlpihmeft 275
Cdd:cd16035 121 AQAVEWlRERGAKNADGKPWFLVVSLVNPH---D---------------I----MFPPDDEERWR--------------- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 276 nVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEP-GSI 354
Cdd:cd16035 164 -RFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGtGQT 242
                       330       340
                ....*....|....*....|....
gi 26986617 355 VPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16035 243 TDALTSHIDLLPTLLGLAGVDAEA 266
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
42-388 8.86e-31

Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293749 [Multi-domain]  Cd Length: 402  Bit Score: 125.63  E-value: 8.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDqdveLG-----------------SLQvmnktrkimeQGGATFTNaFVTTPMCCPSRSSMLTGKYVHNHN 104
Cdd:cd16025   2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRFTN-FHTTALCSPTRAALLTGRNHHQVG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 105 VYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYNGsyiPPGWrewlgliknsrfynytvcrngikek 181
Cdd:cd16025  67 MGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY------------------------- 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 182 hgfdyakdYFTDLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasQHitpsynyAPnmdKHWIM 261
Cdd:cd16025 116 --------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWID 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 262 QYTG---------------------------PMLPIHMEFT--NVL---QRKRLQTLMSV--------DDSVERLYNMLV 301
Cdd:cd16025 161 KYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLK 240
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 302 ESGELDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFIRGPS--IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd16025 241 ELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELA 320
                       410
                ....*....|....*.
gi 26986617 373 GLDSPSDVDGKSVLKL 388
Cdd:cd16025 321 GVEYPKTVNGVPQLPL 336
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
43-418 5.82e-30

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 124.42  E-value: 5.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQD---VELGSLQVMnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSw 117
Cdd:cd16156   1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 118 qamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKE 180
Cdd:cd16156  79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 181 KhgFDYAKDyftdlITNESINYFkmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYN----YAPNMD 256
Cdd:cd16156 153 E--FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYddleNKPLHQ 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 257 KHWIMQYTGP----MLPIHMEFtnvlqrkrLQTLMSVDDSVERLYNMLVEsgELDNTYIIYTADHGYHIGQFGL-VKGKS 331
Cdd:cd16156 222 RLWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLwAKGPA 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 332 MpYDFDIRVPFFIRGPSIEPGSIVPQI-VLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKIwRDT 410
Cdd:cd16156 292 V-YDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATI----------EDPEIPE-NRG 359

                ....*...
gi 26986617 411 FLVERGKF 418
Cdd:cd16156 360 VFVEFGRY 367
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 1.16e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 120.93  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617   42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759   6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759  83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEftnVLQRKRLQTLMS---VDDSVERLYNMLVESGELDNTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDL 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                 ....*.
gi 26986617  392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-389 4.09e-28

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 117.32  E-value: 4.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVE-LGSL-QVMNKTRKI--MEQGGATFTNAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswq 118
Cdd:cd16151   1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 119 amheprTFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYA 187
Cdd:cd16151  77 ------TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 188 KDYFTDLITNESINYFKMSKR-----MYPhrpimMVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM- 261
Cdd:cd16151 148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMv 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 262 QYTgpmlpihmeftnvlqrkrlqtlmsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYD 335
Cdd:cd16151 212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617 336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16151 267 AGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
43-385 1.72e-27

N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.


Pssm-ID: 293753 [Multi-domain]  Cd Length: 393  Bit Score: 115.73  E-value: 1.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQ---DVEL-GSLQVmnKTRKIME--QGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16029   1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR-------EWLGLI-----KNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16029  78 GLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEPA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 184 FDYAKDYFTDLITNESINYFKMSKrmyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPsynyapnmdkhwimqy 263
Cdd:cd16029 156 WDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD---------------- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 264 tgpmlpihmeftnvLQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG------LVKGKSMPYDF 336
Cdd:cd16029 217 --------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNTLWEG 282
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 26986617 337 DIRVPFFIRGPSIEP--GSIVPQIVLNIDLAPTILDIAGLDSPS--DVDGKSV 385
Cdd:cd16029 283 GVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQ 335
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-387 2.39e-23

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 100.91  E-value: 2.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDVElgSLQVMNKTRKIMEQG----------------GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV 105
Cdd:cd16153   1 KPNILWIITDDQRVD--SLSCYNNAHTGKSESrlgyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 106 YtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyipPGWREWLGLIKNSrfyNYTVCRNGIKEKHGF 184
Cdd:cd16153  79 Y-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 185 DYAKdyftdlitnesinyfkmskrmyphrPIMMVISHAAPHGPedsapqfsklypnasqhITPSYNYAPNMDKHWIMQYt 264
Cdd:cd16153 140 DSDK-------------------------PFFVRLSFLQPHTP-----------------VLPPKEFRDRFDYYAFCAY- 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 265 gpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 341
Cdd:cd16153 177 ------------------------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 26986617 342 FFIRGPSIEP---GSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLK 387
Cdd:cd16153 232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-390 2.60e-23

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 103.47  E-value: 2.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  74 GATFTNAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 151
Cdd:cd16150  36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 152 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPIMMVISHAAPHGP-EDS 230
Cdd:cd16150 102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 231 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNvLQR---KRLQTL--------MSVDDSVERLYNM 299
Cdd:cd16150 151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 300 LVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16150 220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
                       330
                ....*....|..
gi 26986617 379 DVDGKSVLKLLD 390
Cdd:cd16150 300 THFGRSLLPVLA 311
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-389 1.78e-22

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 100.12  E-value: 1.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVE------LGSLQVMNKTRKIMEQGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16154   1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 wqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYF 191
Cdd:cd16154  80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 192 TDL----ITNEsinyfkmskrmypHRPIMMVISHAAPHGPedsapqFsklypnasqHITPSYNYAPNMdkhwimqyTGPM 267
Cdd:cd16154 155 TNLaidwIDQQ-------------TKPWFLWLAYNAPHTP------F---------HLPPAELHSRSL--------LGDS 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 268 LPIHMEftnvlqrKR---LQTLMSVDDSVERLYNMLVESgELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFDIR 339
Cdd:cd16154 199 ADIEAN-------PRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGIN 269
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 26986617 340 VPFFIRGPSIEPGSIVPQIVLNI-DLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16154 270 VPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLL 320
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
42-389 1.16e-21

sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293779 [Multi-domain]  Cd Length: 445  Bit Score: 99.04  E-value: 1.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDqdVELGSLQVM-NKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCSSP 115
Cdd:cd16160   1 KPNIVLFFADD--MGYGDLASYgHPTQERgpiddMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEYN---GSYIPpgwrewlgliknsrfynytvcrngikEKHGFDY 186
Cdd:cd16160  77 PWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLP--------------------------SHHGFDF 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 187 A---------------------KD------YFTDLITNESINYFKMSKRMYP----------HRPIMMVISHAAPHGPED 229
Cdd:cd16160 131 VgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVEQPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTPLF 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 230 SAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpmlpihmeftnvlqrkrlqtlMSVddSVERLYNMLVESGELDNT 309
Cdd:cd16160 211 ASKRFK----GKSKR----GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQNT 251
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 310 YIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--V 380
Cdd:cd16160 252 LVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriY 331

                ....*....
gi 26986617 381 DGKSVLKLL 389
Cdd:cd16160 332 DGLSITDLL 340
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
42-422 2.00e-19

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 93.18  E-value: 2.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLtddqdVElgSLQ--VMNKT----------RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKY-VHNHNVYTN 108
Cdd:COG1368 234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 109 NencsspswqAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--Y 186
Cdd:COG1368 306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 187 AKDYFTDLITN-----------ESINYFKMSKRmyphrPIMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNM 255
Cdd:COG1368 352 DREDFDDPFDGgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPE 403
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 256 DKHWIMQYTGPMLpihmeftnvlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhigqfGLVKGKSmPYD 335
Cdd:COG1368 404 EDKKIPDYGKTTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 336 FDI---RVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD-GKSvlkLLDLEKPGNRFR-----TNKKAKI 406
Cdd:COG1368 466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYV 542
                       410
                ....*....|....*.
gi 26986617 407 WRDTFLVERGKFLRKK 422
Cdd:COG1368 543 LKTGELTEEDKELEEE 558
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
43-389 4.51e-19

arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 89.91  E-value: 4.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVELgSLQVMNKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSW 117
Cdd:cd16171   1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 118 QamheprTFAVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLIT 196
Cdd:cd16171  79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVG 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 197 NESinyfkmskrmypHRPIMMvishaaphgpedsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLPiHMEFTN 276
Cdd:cd16171 135 DRS------------TVRVML------------------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLP-HPYPSP 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 277 VLQrkrlQTLMSVDDSVERLYNMLVE--------------SGELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPF 342
Cdd:cd16171 183 SMG----ENFGSIRNIRAFYYAMCAEtdamlgeiisalkdTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPL 257
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 26986617 343 FIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16171 258 LIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
767-816 9.85e-19

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 89.53  E-value: 9.85e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 26986617 767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 816
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
43-373 1.31e-18

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 86.97  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVL-----TDDQDVELGSLQVMNKTRKIMEQGgATFTNAFVTTPMCCPSRS--SMLTGkyvhnhnVYTNNENCSSP 115
Cdd:cd16015   1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTD 193
Cdd:cd16015  73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 194 LITNESINY------FKMSKRMY---PHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDKhwimqyt 264
Cdd:cd16015 128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 265 gpmLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFI 344
Cdd:cd16015 180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
                       330       340
                ....*....|....*....|....*....
gi 26986617 345 RGPSIEPGSIVPQIVLNIDLAPTILDIAG 373
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-389 6.11e-18

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 87.52  E-value: 6.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDV-ELGSLQVMNK-TRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNN---ENCSS 114
Cdd:cd16157   1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNahaRNAYT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 115 PSWQAMHEPRT---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKH 182
Cdd:cd16157  81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 183 GFDYAKDYFTDLITNESiNYfkmsKRMYPHRPIMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimq 262
Cdd:cd16157 158 IGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 263 ytgpmlpihmeFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFG-----LVKGKSMP 333
Cdd:cd16157 217 -----------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTT 285
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26986617 334 YDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16157 286 FEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
43-397 2.07e-17

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 85.96  E-value: 2.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDV-ELG-----SLQVMNKTRkiMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpS 116
Cdd:cd16158   2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQAMHEPRTFAVYLNNTGYRTAFFGKY---LNEyNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkh 182
Cdd:cd16158  79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 183 GFDYAKDYFTDLITNESINYFKMSKRM--YPHRpimmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwi 260
Cdd:cd16158 156 GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD----FIADNA----KEGKPFF--LY-YASHHT-----HYP------- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 261 mQYTGpmlpihMEFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI------GQFGLVK-GKSM 332
Cdd:cd16158 213 -QFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGT 285
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26986617 333 PYDFDIRVPFFIRGPS-IEPGsIVPQIVLNIDLAPTILDIAGLDSPS-DVDGKSVLKLLDLEKPGNR 397
Cdd:cd16158 286 TYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-379 2.98e-17

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 84.51  E-value: 2.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDV-ELGS----LQVMNKTRKI--MEQGGATFTNAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSP 115
Cdd:cd16142   1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 116 SWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDY 186
Cdd:cd16142  73 GLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 187 AKDYFTDLITNE-----SINYFKMSKRMYPHrpimmvishaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwim 261
Cdd:cd16142 139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS---------------PEFEGKSSGKGKYAD------------------- 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 262 qytgpmlpihmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPYD 335
Cdd:cd16142 185 -----------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 26986617 336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD 379
Cdd:cd16142 242 GGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
42-389 8.65e-17

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 84.26  E-value: 8.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDDQDV-ELGSLQvmNKTRK-----IMEQGGATFTNAFVTTPMCCPSRSSMLTGKY------VHNHNVYTNN 109
Cdd:cd16159   1 KPNIVLFMADDLGIgDVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRVIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 110 ENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------------LN-----------------------EY 147
Cdd:cd16159  79 FTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 148 NGSYIPP------------------------GWRE--------------WLGLIKNSRFYNYTVCRNG-IKEKhgfDYAK 188
Cdd:cd16159 154 DLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 189 DYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNmdkhwimqytgpml 268
Cdd:cd16159 231 ENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK----GRSKH----GRYGDN-------------- 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 269 pihmeftnvlqrkrlqtLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YDF 336
Cdd:cd16159 285 -----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEG 347
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26986617 337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16159 348 GIRVPTIVRWPGvIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
43-372 2.13e-14

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 73.61  E-value: 2.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  43 PNIILVLTDDQDVELGSLQVMNKTR----KIMEQGGATFtNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQAMHEP---RTFAVYLNNTGYRTAFFG--KYLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyf 191
Cdd:cd00016  80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE------------------------------TSKEKPFVLF----- 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 192 tdlitnesINYfkmskrmyphrpimmvishAAPHGPedsapqfsklypnasqhitpSYNYAPNMDkhwimqytgpmlpih 271
Cdd:cd00016 125 --------LHF-------------------DGPDGP--------------------GHAYGPNTP--------------- 142
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 272 mEFTNVLQRkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPS 348
Cdd:cd00016 143 -EYYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
                       330       340
                ....*....|....*....|....
gi 26986617 349 IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd00016 214 VKKGGVKHELISQYDIAPTLADLL 237
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
42-389 1.61e-13

arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.


Pssm-ID: 293780 [Multi-domain]  Cd Length: 383  Bit Score: 73.27  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  42 RPNIILVLTDD---QDVELGSLQVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPS 116
Cdd:cd16161   1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 117 WQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TD 193
Cdd:cd16161  80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 194 LITNESINyfkmskrmypHRPIMMVISHAAPHGPEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihme 273
Cdd:cd16161 145 FIQRASAK----------DRPFFLYAALAHVHVPLANLPRF----QSPTSGRGP----------------YG-------- 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 274 ftnvlqrkrlQTLMSVDDSVERLYNMLVESGELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDI 338
Cdd:cd16161 187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 26986617 339 RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16161 257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
67-373 2.26e-08

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 56.05  E-value: 2.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617  67 RKIMEQGGATF--TNAFVT-TpmcCPSRSSMLTGKYVHNHNVYTN-------NENCSSPSWqaMHEPR-----TFAVYLN 131
Cdd:cd16018  26 KRLAEEGVRAKyvKPVFPTlT---FPNHYSIVTGLYPESHGIVGNyfydpktNEEFSDSDW--VWDPWwiggePIWVTAE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 132 NTGYRTA-FFGKY-LNEYNGSYIPPGWREWLGLIKNSRFynytvcrngikekhGFDYAKDYFtdlitnesINYFKMSkrm 209
Cdd:cd16018 101 KAGLKTAsYFWPGsEVAIIGYNPTPIPLGGYWQPYNDSF--------------PFEERVDTI--------LEWLDLE--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 210 yphRPIMMVISHAAPhgpeDSApqfsklypnasQHitpsyNYAPNmdkhwimqytgpmlpiHMEFTNVLQRkrlqtlmsV 289
Cdd:cd16018 156 ---RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------V 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 290 DDSVERLYNMLVESGELDNTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSIEPGSIVPQIvLNIDL 364
Cdd:cd16018 189 DRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDI 258

                ....*....
gi 26986617 365 APTILDIAG 373
Cdd:cd16018 259 YPLMCNLLG 267
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
342-390 1.64e-06

Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 51.44  E-value: 1.64e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 26986617 342 FFIRGPSIEPGSIVPQIVLnIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
229-369 1.17e-05

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 49.13  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 229 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDN 308
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26986617 309 TYIIYTADHGYhigQFGLVKGKSMPY-----DFDIRVPFFIRGPSIEPGSIvPQIVLNIDLAPTIL 369
Cdd:COG3083 456 TIVIITADHGE---EFNENGQNYWGHnsnfsRYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLM 517
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
272-383 8.04e-04

SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 42.90  E-value: 8.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 272 MEFTNVLQ---RKRLQTLMSVDDSVERLYNMLV--ESGEL---------DNTYIIYTADHGyhigqfglvkgksMPYDFD 337
Cdd:cd16016 342 LQMPGVAAaytADELLAGPEPTGIRERLRNGYNpkRSGDLivvlkpgwiEGDGSGKGTTHG-------------SPYDYD 408
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 26986617 338 IRVPFFIRGPSIEPGSIV--PQIVlniDLAPTILDIAGLDSPSDVDGK 383
Cdd:cd16016 409 THVPLLFYGWGIKPGEIPrpVEIT---DIAPTLAALLGIQPPNGCIGK 453
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
283-368 5.08e-03

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 39.88  E-value: 5.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 283 LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSIEPGSI--- 354
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
                        90       100
                ....*....|....*....|.
gi 26986617 355 ------VPQIVLN-IDLAPTI 368
Cdd:cd16020 257 nwgglrLPRHDLDqADLAPLM 277
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
290-375 5.40e-03

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 39.91  E-value: 5.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986617 290 DDSVERLYNMLVESGEldNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSIEPGSIVPQIV 359
Cdd:cd16017 196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
                        90
                ....*....|....*.
gi 26986617 360 LNIDLAPTILDIAGLD 375
Cdd:cd16017 273 SHDNLFHTLLGLLGIK 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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